The structure of cyclolinopeptide A in chloroform refined by RDC measurements. (11th August 2014)

• Record Type: Journal Article
• Authors: Huben, Krzysztof; Jewgiński, Michał; Pabis, Anna; Paluch, Piotr; Luy, Burkhard; Jankowski, Stefan
• Is Part Of: Journal of peptide science. Volume 20:Number 11(2014:Nov.)
• Page Start: 901
• Page End: 907
• Publication Date: 2014-08-11
• Subjects: Peptides -- Periodicals; Peptides -- Periodicals; 572.65
• DOI: 10.1002/psc.2683
• Languages: English
• ISSNs: 1075-2617

Abstract

<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Three‐dimensional structures of molecules traditionally assigned from nuclear Overhauser effects and vicinal coupling constants are recently complemented by measurements of residual dipolar couplings. Residual dipolar couplings measured in a stretched poly(dimethylsiloxane) gel were used to determine the structure of cyclolinopeptide A in chloroform solution at −50 °C. After structure refinement, conformational details of main cluster were discussed in relation to crystal and nuclear Overhauser effect derived structures. Copyright © 2014 European Peptide Society and John Wiley &amp; Sons, Ltd.</p> </abstract>